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Volumn 57, Issue 1-4, 2009, Pages 270-277
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A predominant β-CGTase G1 engineered to elucidate the relationship between protein structure and product specificity
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Author keywords
CGTase; Cyclodextrin; Product specificity; Protein engineering
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Indexed keywords
3-D MODELING;
BACILLUS SP;
CGTASE;
DOUBLE MUTATION;
HIGH COSTS;
HYDROLYSIS ACTIVITY;
KINETIC PROPERTIES;
PRODUCT SPECIFICITY;
PROTEIN ENGINEERING;
PROTEIN STRUCTURES;
RATIONAL DESIGN;
REACTION YIELDS;
SIDE CHAINS;
SINGLE MUTATION;
STARCH HYDROLYSIS;
STERIC HINDRANCES;
SUBSTRATE-BINDING;
TAPIOCA STARCH;
BACTERIOLOGY;
BIOCHEMICAL ENGINEERING;
CYCLIZATION;
GENETIC ENGINEERING;
HYDROLYSIS;
STARCH;
THREE DIMENSIONAL;
DATA STORAGE EQUIPMENT;
BETA CYCLODEXTRIN GLYCOSYLTRANSFERASE G1;
GAMMA CYCLODEXTRIN;
GLYCOSYLTRANSFERASE;
UNCLASSIFIED DRUG;
ARTICLE;
BINDING SITE;
CONTROLLED STUDY;
CYCLIZATION;
ENZYME KINETICS;
ENZYME SPECIFICITY;
ENZYME STRUCTURE;
HYDROLYSIS KINETICS;
MUTAGENESIS;
PROTEIN ENGINEERING;
BACILLUS SP.;
MANIHOT ESCULENTA;
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EID: 68649100448
PISSN: 13811177
EISSN: None
Source Type: Journal
DOI: 10.1016/j.molcatb.2008.09.016 Document Type: Article |
Times cited : (30)
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References (26)
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